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Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor
Considerable evidence implicates gp90MEL as a lymphocyte homing receptor mediating lymphocyte attachment to high endothelial venules of lymph nodes in mouse. The protein appears to function as a calcium- dependent, lectin-like receptor as inferred primarily by the ability of specific carbohydrates t...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1990
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116278/ https://www.ncbi.nlm.nih.gov/pubmed/2202735 |
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collection | PubMed |
description | Considerable evidence implicates gp90MEL as a lymphocyte homing receptor mediating lymphocyte attachment to high endothelial venules of lymph nodes in mouse. The protein appears to function as a calcium- dependent, lectin-like receptor as inferred primarily by the ability of specific carbohydrates to block its function and by the presence of a calcium-type lectin domain in its primary sequence. An ELISA assay is described which provides the first demonstration that the isolated protein has lectin activity and allows a further definition of its carbohydrate specificity. In addition to the monosaccharides mannose-6- phosphate and fructose-1-phosphate, ligand activity is shown for the sulfated glycolipid, sulfatide, and for two sulfated fucose-containing polysaccharides (fucoidin and egg jelly coat) from nonmammalian sources. |
format | Text |
id | pubmed-2116278 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21162782008-05-01 Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor J Cell Biol Articles Considerable evidence implicates gp90MEL as a lymphocyte homing receptor mediating lymphocyte attachment to high endothelial venules of lymph nodes in mouse. The protein appears to function as a calcium- dependent, lectin-like receptor as inferred primarily by the ability of specific carbohydrates to block its function and by the presence of a calcium-type lectin domain in its primary sequence. An ELISA assay is described which provides the first demonstration that the isolated protein has lectin activity and allows a further definition of its carbohydrate specificity. In addition to the monosaccharides mannose-6- phosphate and fructose-1-phosphate, ligand activity is shown for the sulfated glycolipid, sulfatide, and for two sulfated fucose-containing polysaccharides (fucoidin and egg jelly coat) from nonmammalian sources. The Rockefeller University Press 1990-09-01 /pmc/articles/PMC2116278/ /pubmed/2202735 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor |
title | Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor |
title_full | Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor |
title_fullStr | Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor |
title_full_unstemmed | Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor |
title_short | Direct demonstration of the lectin activity of gp90MEL, a lymphocyte homing receptor |
title_sort | direct demonstration of the lectin activity of gp90mel, a lymphocyte homing receptor |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116278/ https://www.ncbi.nlm.nih.gov/pubmed/2202735 |